EC Number   |
Natural Substrates |
|---|
    3.5.99.2 | 4-amino-5-aminomethyl-2-methyl-pyrimidine + H2O |
physiological substrate, hydrolyzed more than two times faster than thiamine. Thiaminase II activity of Thi20p is involved in the thiamine salvage pathway by catalyzing the hydrolysis of 4-amino-5-hydroxymethyl-2-methylpyrimidine precursors in Saccharomyces cerevisiae |
| 3.5.99.2 | 4-amino-5-aminomethyl-2-methylpyrimidine + H2O |
- |
| 3.5.99.2 | more |
THI20 is a trifunctional enzyme that is composed of a ThiD-like N-terminal domain that catalyzes the phosphorylation of 4-amino-5-hydroxymethyl-2-methylpyrimidine to 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate and of 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate to 4-amino-5-hydroxymethyl-2-methylpyrimidine diphosphate, and a TenA-like C-terminal domain with thiaminase activity |
| 3.5.99.2 | more |
no activity with N-formyl-4-amino-5-aminomethyl-2-methylpyrimidine, thiamin monophosphate, thiamin diphosphate, thiamin disulfide, desthiothiamin, and thiochrome |
| 3.5.99.2 | oxothiamin + H2O |
- |
| 3.5.99.2 | oxythiamin + H2O |
- |
| 3.5.99.2 | thiamine + H2O |
- |
